1mi7: Difference between revisions
New page: left|200px<br /><applet load="1mi7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mi7, resolution 2.50Å" /> '''Crystal Structure of... |
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[[Image:1mi7.gif|left|200px]]<br /><applet load="1mi7" size=" | [[Image:1mi7.gif|left|200px]]<br /><applet load="1mi7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1mi7, resolution 2.50Å" /> | caption="1mi7, resolution 2.50Å" /> | ||
'''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol'''<br /> | '''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol'''<br /> | ||
==Overview== | ==Overview== | ||
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA | The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol. | ||
==About this Structure== | ==About this Structure== | ||
1MI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1MI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Benoff, B.]] | [[Category: Benoff, B.]] | ||
[[Category: Berger, T.]] | [[Category: Berger, T.]] | ||
[[Category: Berman, H | [[Category: Berman, H M.]] | ||
[[Category: Carey, J.]] | [[Category: Carey, J.]] | ||
[[Category: Lawson, C | [[Category: Lawson, C L.]] | ||
[[Category: IPA]] | [[Category: IPA]] | ||
[[Category: alcohol induced conformational rearrangement]] | [[Category: alcohol induced conformational rearrangement]] | ||
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[[Category: domain swapping]] | [[Category: domain swapping]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:25 2008'' |
Revision as of 14:55, 21 February 2008
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Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol
OverviewOverview
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.
About this StructureAbout this Structure
1MI7 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
E. coli trp repressor forms a domain-swapped array in aqueous alcohol., Lawson CL, Benoff B, Berger T, Berman HM, Carey J, Structure. 2004 Jun;12(6):1099-108. PMID:15274929
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